Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
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London: Nature Publishing Group UK
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Language
English
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London: Nature Publishing Group UK
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Contents
Tissue deposition of soluble proteins as amyloid fibrils underlies a range of fatal diseases. The two naturally occurring human lysozyme variants are both amyloidogenic, and are shown here to be unstable. They aggregate to form amyloid fibrils with transformation of the mainly helical native fold, observed in crystal structures, to the amyloid fibr...
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Full title
Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
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TN_cdi_proquest_miscellaneous_78822602
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_78822602
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ISSN
0028-0836
E-ISSN
1476-4687
DOI
10.1038/385787a0
